6HM1
Structural and thermodynamic signatures of ligand binding to an enigmatic chitinase-D from Serratia proteamaculans
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-06-22 |
| Detector | DECTRIS PILATUS3 S 6M |
| Wavelength(s) | 0.97319 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 60.777, 62.855, 103.183 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 43.690 - 1.540 |
| R-factor | 0.1706 |
| Rwork | 0.169 |
| R-free | 0.20300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4nzc |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.829 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((1.10.1_2155: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 43.690 | 1.600 |
| High resolution limit [Å] | 1.540 | 1.540 |
| Rmerge | 0.054 | 0.603 |
| Number of reflections | 57471 | 5508 |
| <I/σ(I)> | 12.5 | 1.8 |
| Completeness [%] | 96.9 | 96.2 |
| Redundancy | 3.3 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 298 | 0.2 M magnesium chloride, 0.1 M Tris pH 8.5 and 20% (w/v) PEG 8000 |
